TY  - JOUR
AU  - Anđelković, Uroš
AU  - Picuric, Srdjan
AU  - Vujčić, Zoran
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1052
AB  - Four external invertase isoforms (EINV1, EINV2, EINV3 and EINV4) from Saccharomyces cerevisiae were highly purified by isoelectric precipitation, ethanol precipitation, ion-exchange on QAE-Sephadex and gel filtration using Sephacryl S-200. Unlike previously published procedures for external invertase purification, a specially designed step elution was applied on QAE-Sephadex which enabled the separation of four isoforms. The isoforms have the same molecular mass and catalytic properties: K-m for sucrose (25.6 mM), pH optimum (3.5-5.0) and temperature optimum (60 degrees C), but they exhibit significant difference in pl values, thermal stability and chemical reactivity. Deglycosylation Studies showed that the observed differences between isoforms arise from posttranslational modifications. Results showed that external invertase is a mixture of at least four isoforms, but in order to improve the efficiency of food industry processes, only the most stable isoform (EINV1) should be purified and utilised. Substantially different chemical reactivity of the isoforms could be used to improve the yield of covalent immobilization procedures. (C) 2009 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms
VL  - 120
IS  - 3
SP  - 799
EP  - 804
DO  - 10.1016/j.foodchem.2009.11.013
ER  - 

@article{
author = "Anđelković, Uroš and Picuric, Srdjan and Vujčić, Zoran",
year = "2010",
abstract = "Four external invertase isoforms (EINV1, EINV2, EINV3 and EINV4) from Saccharomyces cerevisiae were highly purified by isoelectric precipitation, ethanol precipitation, ion-exchange on QAE-Sephadex and gel filtration using Sephacryl S-200. Unlike previously published procedures for external invertase purification, a specially designed step elution was applied on QAE-Sephadex which enabled the separation of four isoforms. The isoforms have the same molecular mass and catalytic properties: K-m for sucrose (25.6 mM), pH optimum (3.5-5.0) and temperature optimum (60 degrees C), but they exhibit significant difference in pl values, thermal stability and chemical reactivity. Deglycosylation Studies showed that the observed differences between isoforms arise from posttranslational modifications. Results showed that external invertase is a mixture of at least four isoforms, but in order to improve the efficiency of food industry processes, only the most stable isoform (EINV1) should be purified and utilised. Substantially different chemical reactivity of the isoforms could be used to improve the yield of covalent immobilization procedures. (C) 2009 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms",
volume = "120",
number = "3",
pages = "799-804",
doi = "10.1016/j.foodchem.2009.11.013"
}

Anđelković, U., Picuric, S.,& Vujčić, Z.. (2010). Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms. in Food Chemistry
Elsevier Sci Ltd, Oxford., 120(3), 799-804.
https://doi.org/10.1016/j.foodchem.2009.11.013

Anđelković U, Picuric S, Vujčić Z. Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms. in Food Chemistry. 2010;120(3):799-804.
doi:10.1016/j.foodchem.2009.11.013 .

Anđelković, Uroš, Picuric, Srdjan, Vujčić, Zoran, "Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms" in Food Chemistry, 120, no. 3 (2010):799-804,
https://doi.org/10.1016/j.foodchem.2009.11.013 . .